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Q27772

- C1TC_SPOFR

UniProt

Q27772 - C1TC_SPOFR

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Protein
C-1-tetrahydrofolate synthase, cytoplasmic
Gene
N/A
Organism
Spodoptera frugiperda (Fall armyworm)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at transcript leveli

Functioni

Catalytic activityi

5,10-methylenetetrahydrofolate + NADP+ = 5,10-methenyltetrahydrofolate + NADPH.UniRule annotation
5,10-methenyltetrahydrofolate + H2O = 10-formyltetrahydrofolate.UniRule annotation
ATP + formate + tetrahydrofolate = ADP + phosphate + 10-formyltetrahydrofolate.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei195 – 1951NADP By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi170 – 1723NADP By similarity
Nucleotide bindingi378 – 3858ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. formate-tetrahydrofolate ligase activity Source: UniProtKB-EC
  3. methenyltetrahydrofolate cyclohydrolase activity Source: UniProtKB-EC
  4. methylenetetrahydrofolate dehydrogenase (NADP+) activity Source: UniProtKB-EC

GO - Biological processi

  1. folic acid-containing compound biosynthetic process Source: InterPro
  2. histidine biosynthetic process Source: UniProtKB-KW
  3. methionine biosynthetic process Source: UniProtKB-KW
  4. purine nucleotide biosynthetic process Source: UniProtKB-KW
  5. tetrahydrofolate interconversion Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Ligase, Oxidoreductase

Keywords - Biological processi

Amino-acid biosynthesis, Histidine biosynthesis, Methionine biosynthesis, One-carbon metabolism, Purine biosynthesis

Keywords - Ligandi

ATP-binding, NADP, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00193.

Names & Taxonomyi

Protein namesi
Recommended name:
C-1-tetrahydrofolate synthase, cytoplasmic
Short name:
C1-THF synthase
Including the following 3 domains:
Methylenetetrahydrofolate dehydrogenase (EC:1.5.1.5)
Methenyltetrahydrofolate cyclohydrolase (EC:3.5.4.9)
Formyltetrahydrofolate synthetase (EC:6.3.4.3)
OrganismiSpodoptera frugiperda (Fall armyworm)
Taxonomic identifieri7108 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaLepidopteraGlossataDitrysiaNoctuoideaNoctuidaeAmphipyrinaeSpodoptera

Subcellular locationi

Cytoplasm By similarity UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 933933C-1-tetrahydrofolate synthase, cytoplasmicUniRule annotation
PRO_0000199325Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ27772.
SMRiQ27772. Positions 10-294, 467-528.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 303303Methylenetetrahydrofolate dehydrogenase and cyclohydrolaseUniRule annotation
Add
BLAST
Regioni51 – 555Substrate binding By similarity
Regioni98 – 1003Substrate binding By similarity
Regioni270 – 2745Substrate binding By similarity
Regioni304 – 933630Formyltetrahydrofolate synthetaseUniRule annotation
Add
BLAST

Domaini

This trifunctional enzyme consists of two major domains: an N-terminal part containing the methylene-THF dehydrogenase and cyclohydrolase activities and a larger C-terminal part containing formyl-THF synthetase activity.UniRule annotation

Sequence similaritiesi

In the N-terminal section; belongs to the tetrahydrofolate dehydrogenase/cyclohydrolase family.
In the C-terminal section; belongs to the formate--tetrahydrofolate ligase family.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
3.40.50.720. 1 hit.
HAMAPiMF_01543. FTHFS.
MF_01576. THF_DHG_CYH.
InterProiIPR000559. Formate_THF_ligase.
IPR020628. Formate_THF_ligase_CS.
IPR016040. NAD(P)-bd_dom.
IPR027417. P-loop_NTPase.
IPR000672. THF_DH/CycHdrlase.
IPR020630. THF_DH/CycHdrlase_cat_dom.
IPR020867. THF_DH/CycHdrlase_CS.
IPR020631. THF_DH/CycHdrlase_NAD-bd_dom.
[Graphical view]
PfamiPF01268. FTHFS. 1 hit.
PF00763. THF_DHG_CYH. 1 hit.
PF02882. THF_DHG_CYH_C. 1 hit.
[Graphical view]
PRINTSiPR00085. THFDHDRGNASE.
SUPFAMiSSF52540. SSF52540. 2 hits.
PROSITEiPS00721. FTHFS_1. 1 hit.
PS00722. FTHFS_2. 1 hit.
PS00766. THF_DHG_CYH_1. 1 hit.
PS00767. THF_DHG_CYH_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q27772-1 [UniParc]FASTAAdd to Basket

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MWEPQGSLDP VLESIENELR DQVAEARSRW AGFDARLAIV QVGGREDSNV    50
YIRMKLRAAE NIGITAEHIQ LPRDITETEL LANITSLNES PYVHGIIVQM 100
PLDSVHPIDS HAITDAVSPD KDVDGLNTIN EGRVRVGDLS GFIPCTPAGC 150
VELIKRTGVT IAGKNVVVLG RSRIVGTPVS ELLKWEHATV TVCHSKTKNL 200
SEITKTADIL VVAIGRGEMV RGSWIKPGAV VIDCGINPIS DPTKKSGQRL 250
VGDVAYEEAV QVASHVTPVP GGVGPMTVAM LMRNTVQAAR RQLDRLLAPT 300
WPLRPLRITP LSPPPSDIVI ARSQKPKDIS ELAHEIGLFS NEVSQYGRTK 350
AKISLSVLDR MRNQQGAKYI VVAGITPTPL GEGKSTTLLG LVQALSAHRG 400
RNSFAVMRQP SQGPTFGVKG GAAGGGYSQV IPMEEFNLHL TGDIHAGTAA 450
NNLLAAQMDA RIFHELTQKD GPLFDRLVPK IKGVRKFSPI QLRRLKRLGI 500
TKTDPDTLTE GEKSKFARLN IDTSKIMWNR VVDLNDRYLR KITVGQSPTE 550
KGFTRETAFD ISVASEIMAI LALGRDVEDI KERLANMVVA LDKSGNPVTA 600
DDLGMTGALL VLLRDAFEPT LMQSLEGTPV LVHTGPFANI RHGCSSILAD 650
KIAMKLAGEN GYVATEAGFG SDIGMEKFFD IKCRASGDTP HCAVIVSTVR 700
ALKMHGGGPP VSAGMPLNDV YVQENLELLS KGLCNLGKHI SNGNKFGVPV 750
VVAINKHGND TPAELNLVKE FAVKNGAFRA VLCDHWAKGG LGALELADAV 800
IEACDSKSKF DFLYPLQLSI QEKIQIIAKE MYGAGQVEYT DEVLEKIKTF 850
TDMGYDKFPI CMAKTSNSLT GDPAVKGAPT GFTLKINGIF ASVGAGFVVP 900
MVGEISKMPG LPTRPSIYDI DLNTKTGEIE GLF 933
Length:933
Mass (Da):100,618
Last modified:January 16, 2004 - v3
Checksum:i55C3FA820C1A55CB
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L36189 mRNA. Translation: AAA74302.1.
PIRiS53523.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L36189 mRNA. Translation: AAA74302.1 .
PIRi S53523.

3D structure databases

ProteinModelPortali Q27772.
SMRi Q27772. Positions 10-294, 467-528.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00193 .

Family and domain databases

Gene3Di 3.40.50.300. 2 hits.
3.40.50.720. 1 hit.
HAMAPi MF_01543. FTHFS.
MF_01576. THF_DHG_CYH.
InterProi IPR000559. Formate_THF_ligase.
IPR020628. Formate_THF_ligase_CS.
IPR016040. NAD(P)-bd_dom.
IPR027417. P-loop_NTPase.
IPR000672. THF_DH/CycHdrlase.
IPR020630. THF_DH/CycHdrlase_cat_dom.
IPR020867. THF_DH/CycHdrlase_CS.
IPR020631. THF_DH/CycHdrlase_NAD-bd_dom.
[Graphical view ]
Pfami PF01268. FTHFS. 1 hit.
PF00763. THF_DHG_CYH. 1 hit.
PF02882. THF_DHG_CYH_C. 1 hit.
[Graphical view ]
PRINTSi PR00085. THFDHDRGNASE.
SUPFAMi SSF52540. SSF52540. 2 hits.
PROSITEi PS00721. FTHFS_1. 1 hit.
PS00722. FTHFS_2. 1 hit.
PS00766. THF_DHG_CYH_1. 1 hit.
PS00767. THF_DHG_CYH_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Primary structure of a folate-dependent trifunctional enzyme from Spodoptera frugiperda."
    Tremblay G.B., MacKenzie R.E.
    Biochim. Biophys. Acta 1261:129-133(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Ovary.

Entry informationi

Entry nameiC1TC_SPOFR
AccessioniPrimary (citable) accession number: Q27772
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: January 16, 2004
Last modified: April 16, 2014
This is version 81 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

Multifunctional enzyme

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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